Literature DB >> 24287282

Strike a pose: Gαq complexes at the membrane.

Angeline M Lyon1, Veronica G Taylor1, John J G Tesmer2.   

Abstract

The heterotrimeric G protein Gαq is a central player in signal transduction, relaying signals from activated G-protein-coupled receptors (GPCRs) to effectors and other proteins to elicit changes in intracellular Ca(2+), the actin cytoskeleton, and gene transcription. Gαq functions at the intracellular surface of the plasma membrane, as do its best-characterized targets, phospholipase C-β, p63RhoGEF, and GPCR kinase 2 (GRK2). Recent insights into the structure and function of these signaling complexes reveal several recurring themes, including complex multivalent interactions between Gαq, its protein target, and the membrane, that are likely essential for allosteric control and maximum efficiency in signal transduction. Thus, the plasma membrane is not only a source of substrates but also a key player in the scaffolding of Gαq-dependent signaling pathways.
Copyright © 2013 Elsevier Ltd. All rights reserved.

Entities:  

Keywords:  ARHGEF25; G-protein-coupled receptor; GRK2; Gα(q); crystallography; heterotrimeric G protein signaling; membrane; p63RhoGEF; phospholipase Cβ; phospholipids; protein structure; second messengers

Mesh:

Substances:

Year:  2013        PMID: 24287282      PMCID: PMC3880608          DOI: 10.1016/j.tips.2013.10.008

Source DB:  PubMed          Journal:  Trends Pharmacol Sci        ISSN: 0165-6147            Impact factor:   14.819


  70 in total

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4.  BRET-based effector membrane translocation assay monitors GPCR-promoted and endocytosis-mediated Gq activation at early endosomes.

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5.  Dissociation of the G protein βγ from the Gq-PLCβ complex partially attenuates PIP2 hydrolysis.

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9.  PLCβ3 mediates cortactin interaction with WAVE2 in MCP1-induced actin polymerization and cell migration.

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